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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| VAG0344-100 | 7 days | 100 µg | $400.00 |
Select product before adding to cart
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| VAG0344-0.5 | 7 days | 0.5 mg | $1,600.00 | |||
| VAG0344-1 | 7 days | 1 mg | $2,240.00 |
Product Overview | |
| Name | HIV-1/2 Rapid |
|---|---|
| Description | |
| HIV-1/2 Rapid Test Recombinant | |
| Introduction | |
| HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids. Immunodeficiency develops more slowly with HIV-2. HIV-2 is less infectious in the early stages of the virus than with HIV-1. The infectiousness of HIV-2 increases as the virus progresses. Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion. HIV-1 gp41 helical regions can form more stable 6-helix bundles than HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition. | |
| Source | |
| Escherichia Coli. | |
| Physical Appearance | |
| Sterile filtered colorless clear solution. | |
| Formulation | |
| 50mM Tris-HCl & 6M urea, pH 7.2. | |
| Stability | |
| HIV-2 Envelope although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles. | |
| Purity | |
| Greater than 95.0% as determined by HPLC analysis and SDS-PAGE. | |
| Applications | |
| HIV-2 Envelope antigen in ELISA and Western blots, excellent antigen for early detection of HIV seroconvertors with minimal specificity problems. | |
| Specificity | |
| Immunoreactive with all sera of HIV-2 infected individuals. | |
| Precautions | |
| HIV-1/2 Rapid is for research use only and not for use in diagnostic or therapeutic procedures. | |
Background |
The Human Immunodeficiency Virus (HIV), specifically HIV-1 and HIV-2, continues to pose significant global health challenges, necessitating constant efforts to understand the intricacies of viral replication, immune evasion, and potential therapeutic interventions. In this pursuit, Recombinant HIV-1/2 Proteins serve as indispensable tools for researchers, offering a controlled environment to dissect viral components and study their interactions with the host immune system. This research embarks on a comprehensive exploration of Recombinant HIV-1/2 Proteins, shedding light on their structural attributes, immunogenic properties, and potential applications in antiviral drug development. By delving into the properties of these recombinant proteins, scientists aim to deepen our understanding of HIV pathogenesis and pave the way for innovative strategies in HIV treatment and prevention. Structural Insights into Recombinant HIV-1/2 Proteins: Recombinant HIV-1/2 Proteins, derived from various viral components such as envelope glycoproteins (gp120, gp41), reverse transcriptase, and integrase, provide a controlled system for studying the virus's structural nuances. Understanding the three-dimensional structure of these proteins is pivotal for deciphering how the virus engages with host cells, evades immune responses, and undergoes dynamic structural changes during its life cycle. Immunogenic Properties and Vaccine Development: The immunogenicity of Recombinant HIV-1/2 Proteins makes them invaluable in the quest for an effective HIV vaccine. These proteins, when presented to the immune system, mimic key viral components, inducing specific immune responses. Studying the immunogenic properties of these recombinant proteins aids in the design and evaluation of potential vaccine candidates, with the ultimate goal of eliciting robust and broadly neutralizing antibodies against HIV. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from ADMEbio to advance their research.
Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
Thank you,
ADMEbio Team
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ADMEbio Team
